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Related Concept Videos

Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Activation of Integrins01:15

Activation of Integrins

Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
Integrins01:10

Integrins

Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Tension Response at Adherens Junctions01:26

Tension Response at Adherens Junctions

The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin homology) domains...
Catenins01:23

Catenins

Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the adherens...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...

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Related Experiment Video

Updated: Jun 26, 2026

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
09:14

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

Published on: June 13, 2014

Mechanisms that regulate adaptor binding to beta-integrin cytoplasmic tails.

Kyle R Legate1, Reinhard Fässler

  • 1Department of Molecular Medicine, Max Planck Institute of Biochemistry, Martinsried, Germany. legate@biochem.mpg.de

Journal of Cell Science
|January 2, 2009
PubMed
Summary

Cells use adaptor proteins to regulate integrin function, connecting the extracellular matrix to the cytoskeleton. These adaptors

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Last Updated: Jun 26, 2026

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
09:14

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Published on: June 13, 2014

Analyzing Cell Surface Adhesion Remodeling in Response to Mechanical Tension Using Magnetic Beads
07:55

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Published on: March 8, 2017

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules
08:15

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules

Published on: October 17, 2014

Area of Science:

  • Cell biology
  • Molecular biology
  • Biochemistry

Background:

  • Cells interact with their environment via transmembrane receptors like integrins.
  • Integrins link the extracellular matrix to the cytoskeleton, influencing cell physiology.
  • Integrins lack intrinsic enzymatic or actin-binding activity, requiring adaptor molecules.

Purpose of the Study:

  • To discuss adaptor proteins that bind to beta integrin tails.
  • To explain how the binding of these adaptors is regulated.

Main Methods:

  • Review of literature on integrin adaptor proteins.
  • Focus on talin, tensin, filamin, 14-3-3, and integrin-linked kinase (ILK) as examples.

Main Results:

  • Adaptor proteins mediate integrin functions by binding to their cytoplasmic tails.
  • Regulatory mechanisms control the spatial and temporal binding of adaptors to integrin tails.
  • Competition for binding sites necessitates regulated adaptor recruitment.

Conclusions:

  • Adaptor protein binding to beta integrins is tightly regulated.
  • Understanding these regulatory mechanisms is crucial for cell signaling research.